Edge Rewrite
// HTMLRewriter · presentation

This page was redesigned at the edge.

Cloudflare fetched the original article and streamed it through HTMLRewriter to apply an entirely new visual system without rebuilding the source page.

// request.cf · coarse context

A page that knows where it met you.

Only coarse request metadata is shown. This demo does not display or persist visitor IP addresses.

Country
US
Cloudflare location
CMH
Connection
HTTP/2
Language
Not provided

Ray ID: a4078c4fcb1224ea

Jump to content

Replication protein A3

From Wikipedia, the free encyclopedia
(Redirected from RPA3)

RPA3
Identifiers
AliasesRPA3, REPA3, RP-A p14, replication protein A3
External IDsOMIM: 179837; MGI: 1915490; GeneCards: RPA3
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002947

NM_026632

RefSeq (protein)

NP_002938

NP_080908

Location (UCSC)Chr 7: 7.64 – 7.72 MbChr 6: 8.26 – 8.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Replication protein A 14 kDa subunit is a protein that in humans is encoded by the RPA3 gene.[5][6] RPA is a single-stranded DNA-binding protein that is conserved in eukaryotes and plays essential roles in the metabolism of nucleic acids.[7] Unlike helicase, RPA does not separate strands but binds and protects exposed single-stranded DNA to prevent secondary structure formation and degradation.[8] RPA is usually considered to be the functional equivalent of bacterial single-stranded DNA-binding proteins (SSB), although it is much more complex structurally in eukaryotic cells.[9]

Interactions

[edit]

RPA3 has been shown to interact with replication protein A1[10][11] and replication protein A2.[10][11] Together, they form a heterotrimeric complex that contributes to the direct binding of single-stranded DNA during replication, homologous recombination, nucleoetide excision repair, and mismatch repair.[12] RPA3 can directly contact ssDNA on the 3' side of a substrate, and this polarity is crucial for the positioning and stability of nucleases that are involved in excision repair[13]

See also

[edit]

References

[edit]
  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000106399 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000012483 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Umbricht CB, Erdile LF, Jabs EW, Kelly TJ (March 1993). "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A". The Journal of Biological Chemistry. 268 (9): 6131–6138. doi:10.1016/S0021-9258(18)53229-4. PMID 8454588.
  6. ↑ "Entrez Gene: RPA3 replication protein A3, 14kDa".
  7. ↑ Salas TR, Petruseva I, Lavrik O, Saintomé C (January 2009). "Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA". Nucleic Acids Research. 37 (1): 38–46. doi:10.1093/nar/gkn895. PMC 2615627. PMID 19010961.
  8. ↑ Chen R, Wold MS (December 2014). "Replication protein A: single-stranded DNA's first responder: dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair". BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology. 36 (12): 1156–1161. doi:10.1002/bies.201400107. PMC 4629251. PMID 25171654.
  9. ↑ Iftode C, Daniely Y, Borowiec JA (1999). "Replication protein A (RPA): the eukaryotic SSB". Critical Reviews in Biochemistry and Molecular Biology. 34 (3): 141–180. doi:10.1080/10409239991209255. PMID 10473346.
  10. 1 2 Bochkareva E, Frappier L, Edwards AM, Bochkarev A (February 1998). "The RPA32 subunit of human replication protein A contains a single-stranded DNA-binding domain". The Journal of Biological Chemistry. 273 (7): 3932–3936. doi:10.1074/jbc.273.7.3932. PMID 9461578.
  11. 1 2 Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A (April 2002). "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA". The EMBO Journal. 21 (7): 1855–1863. doi:10.1093/emboj/21.7.1855. PMC 125950. PMID 11927569.
  12. ↑ Madru C, Martínez-Carranza M, Laurent S, Alberti AC, Chevreuil M, Raynal B, et al. (April 2023). "DNA-binding mechanism and evolution of replication protein A". Nature Communications. 14 (1) 2326. Bibcode:2023NatCo..14.2326M. doi:10.1038/s41467-023-38048-w. PMC 10122647. PMID 37087464.
  13. ↑ de Laat WL, Appeldoorn E, Sugasawa K, Weterings E, Jaspers NG, Hoeijmakers JH (August 1998). "DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair". Genes & Development. 12 (16): 2598–2609. doi:10.1101/gad.12.16.2598. PMC 317078. PMID 9716411.

Further reading

[edit]